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Amyloid Fibrils And Prefibrillar Aggregates
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Book Synopsis Amyloid Fibrils and Prefibrillar Aggregates by : Daniel Erik Otzen
Download or read book Amyloid Fibrils and Prefibrillar Aggregates written by Daniel Erik Otzen and published by John Wiley & Sons. This book was released on 2013-06-04 with total page 496 pages. Available in PDF, EPUB and Kindle. Book excerpt: Summing up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher organisms. For Biochemists, Molecular Biologists, Neurobiologists, Neurophysiologists and those working in the Pharmaceutical Industry.
Book Synopsis Amyloid, Prions, and Other Protein Aggregates, Part C by :
Download or read book Amyloid, Prions, and Other Protein Aggregates, Part C written by and published by Elsevier. This book was released on 2006-10-06 with total page 412 pages. Available in PDF, EPUB and Kindle. Book excerpt: The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part B (volume 412) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies. Presents detailed protocols Includes troubleshooting tips Provides coverage on structural biology, computational methods, and biology
Book Synopsis Analysis of Beta-amyloid Aggregation and Amyloid Precursor Protein Dimerization by : Paul M. Gorman
Download or read book Analysis of Beta-amyloid Aggregation and Amyloid Precursor Protein Dimerization written by Paul M. Gorman and published by . This book was released on 2006 with total page 348 pages. Available in PDF, EPUB and Kindle. Book excerpt: Alzheimer's Disease (AD) is a neuropathological disorder characterized by the progressive deposition of insoluble amyloid plaques and vascular deposits consisting primarily of 4.5 kDa amyloid beta peptides (Abeta). There is increasing evidence that the deposition of Abeta fibrils in the brain, an invariable feature of AD, and/or prefibrillar aggregates likely cause neurodegeneration in AD. While Abeta fibrils were a previous research focus, recent experiments implicate prefibrillar aggregates as the toxic species. The identification and characterization of prefibrillar aggregates is of great importance to understanding AD and the development of therapeutic strategies. Biophysical and spectroscopic techniques were used to examine the effects of electrostatic interactions on Abeta oligomerization. Experimental work demonstrated that, while salt bridges likely provide stability to preformed Abeta aggregates, these interactions are not essential for the early stages of aggregation. Abeta oligomerization is driven by the formation of pH-independent interactions and is impeded by electrostatic repulsion at pH values away from the isoelectric point. Diffuse plaques, containing only the 42-residue form of Abeta, are unstructured and non-toxic; they appear before toxic senile plaques containing both 40 and 42-residue forms. Through incubation, Abeta40 and Abeta42 were shown to co-incorporate into unstructured aggregates early during fibrillogenesis later leading to tightly packed aggregates with secondary structure. Previously, the stage at which the Abeta variants co-incorporated during the fibrillogenic process was unknown. After observing that the amyloid precursor protein transmembrane (APP-TM) domain contains two known dimerization motifs (GXXXG/A), oligomerization of the APP-TM domain was examined. A model system was developed to investigate the effects of familial AD mutations on the dimerization propensity of APP-TM domains. This work culminated in the first experimentally supported mechanism to explain how genetic mutations within the APP gene lead to the observed phenotype and predisposition to AD. Further experimentation led to the discovery of non-denaturing detergents that stabilize suspected on-pathway spherical Abeta aggregates. These detergent-stabilized Abeta oligomers share many of the structural features and biological activities of both membrane bound Abeta and spherical oligomers of Abeta formed in solution. Thus, these stabilizing detergents may prove useful in high-resolution structural analysis of spherical oligomers.
Book Synopsis Bio-nanoimaging by : Vladimir N Uversky
Download or read book Bio-nanoimaging written by Vladimir N Uversky and published by Academic Press. This book was released on 2013-11-05 with total page 556 pages. Available in PDF, EPUB and Kindle. Book excerpt: Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers - Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties. Provides practical examples of nanoimaging research from leading molecular biology, cell biology, protein chemistry, biotechnology, genetics, and pharmaceutical labs Includes over 200 color images to illustrate the power of various nanoimaging technologies Focuses on nanoimaging techniques applied to protein misfolding and aggregation in molecular medicine
Book Synopsis The Nature and Origin of Amyloid Fibrils by : Gregory R. Bock
Download or read book The Nature and Origin of Amyloid Fibrils written by Gregory R. Bock and published by John Wiley & Sons. This book was released on 2008-04-30 with total page 266 pages. Available in PDF, EPUB and Kindle. Book excerpt: Amyloid fibrils are associated with a range of pathological disorders including Alzheimer's Disease, Down's syndrome, diabetes, cardiomyopathies, and transmissible spongiform encephalopathies. This volume is a comprehensive account of recent developments in the understanding of the process of amyloid fibrils. Contains up-to-date data on all of the clinical problems which, despite their pathological significance, are still largely unsolved.
Book Synopsis Biophysical Inquiry Into Protein Aggregation And Amyloid Diseases by : Pier Luigi San Biagio
Download or read book Biophysical Inquiry Into Protein Aggregation And Amyloid Diseases written by Pier Luigi San Biagio and published by . This book was released on 2008-01-01 with total page 267 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book collects papers by biology, chemistry and physics researchers all actively working in the field of protein aggregation as related to amyloid diseases. Protein precipitates having a highly ordered, fibril-like structure accompany several fatal diseases, such as Alzheimer's, Parkinson's, Creutzfeldt-Jacob and Huntington diseases. Amyloid fibrils associated to different diseases share a common cross beta repeat structure, despite the lack of sequence homologies and structure similarities in the relative proteins. About 20 proteins are known to form amyloid fibrils under physiological conditions. In any of them a conformational change into an unfolding intermediate seems to be responsible for amyloid fibrils formation. A growing body of evidence indicates that in vitro any protein or polypeptide can assembly into fibrillar structures under mildly denaturing conditions, where metastable unfolding intermediates become stabilized. These findings have added further interest to the outstanding problem of protein folding/unfolding and aggregation, whose high interdisciplinary character touches upon biology, chemistry and physics. Indeed, only by joining different expertise we may hope to achieve a unifying view of protein aggregation mechanism in terms of a few general principles. A central issue in the problem of amyloid formation is the understanding of the thermodynamic transitions governing this type of self-organization process in which the symmetry of the interacting molecules should play a relevant role. The first paper of this volume by Manno deals with the modeling of amyloid formation in the frame of physics of colloidal coagulation, and highlights those theoretical aspects that can be investigated by experiments in vitro. The relevance of crowding and confinement, or a combination of them, on the aggregation of proteins in living system is discussed in the paper of Temussi, where results obtained from studies in vitro and in vivo are revised and compared. The paper by Higuchi et al. addresses the theme of disease transmission in living organisms. The authors present the case of systemic amyloidosis in mice showing that pre-formed amyloid fibrils injected in, or ingested by, mice susceptible to infection are capable to accelerate amyloid deposition. A new emerging hypothesis on the onset of amyloid diseases points out the role played by small oligomeric species representing early pre-fibrillar intermediates. Such small aggregates have been observed in the case of beta-peptide responsible for Alzheimer disease. The paper by Di Carlo et al. describes the toxic properties of beta-peptide aggregates with different size, and indicates the possible degeneration pathways leading to the disease. If pre-fibrillar small oligomers are amyloid intermediates, inhibiting their formation should be an important target for therapeutic strategies. The paper by Sgarbossa et al. illustrates the potential use of small polycyclic aromatic molecules that can act as fibrillogenesis inhibitors by imposing unfavorable conformational constraints to the aggregating molecules. The paper by Pastore discusses the aggregation properties of proteins having homo-polymeric stretches, whose tract length determines the onset of the pathologies. The most famous of them is the Huntington disease associated to expansion of polyglutamine repeat. Bisaglia et al. revised the case of alpha-synuclein involved in Parkinson disease. The paper describes the capacity of this protein of adopting different conformations as a response to the environments, with relation to its physiological function or possible pathological role. Finally, two papers concern the role of metal ions on protein aggregation. The paper by Morante gives a review of the possible harmful or useful effects of some metal ions on two pathological proteins, examined through the synergic use of computational and experimental techniques. The paper by Militello et al. describes metal effects on the conformational change and structural properties of aggregates of beta-lactoglobulin and bovine serum albumin, taken as convenient model systems for studying protein aggregation. We thank the contributing authors for having provide altogether a wide perspective, multi-faceted survey of the conceptual and experimental tools that can be applied for unraveling the mechanism of protein aggregation.
Book Synopsis Early Stage Protein Misfolding and Amyloid Aggregation by :
Download or read book Early Stage Protein Misfolding and Amyloid Aggregation written by and published by Academic Press. This book was released on 2017-01-18 with total page 322 pages. Available in PDF, EPUB and Kindle. Book excerpt: Early Stage Protein Misfolding and Amyloid Aggregation, Volume 329, the latest in the International Review of Cell and Molecular Biology series presents comprehensive reviews and current advances in cell and molecular biology, including articles that address the structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. The series has a worldwide readership and maintains a high standard by publishing invited articles on important and timely topics as authored by prominent cell and molecular biologists. Provides comprehensive reviews and current advances Presents a wide range of perspectives on specific subjects Includes valuable reference material for advanced undergraduates, graduate students, and professional scientists
Book Synopsis The Hidden World of Protein Aggregation by :
Download or read book The Hidden World of Protein Aggregation written by and published by Elsevier. This book was released on 2024-05-30 with total page 530 pages. Available in PDF, EPUB and Kindle. Book excerpt: The Hidden World of Protein Aggregation, Volume 206 provides a comprehensive exploration of protein aggregation, uncovering the factors behind the formation of amorphous aggregates and ordered structures called amyloid fibrils. It delves into the advantages and disadvantages of protein aggregates, addressing topics such as cytotoxicity and disorders linked to misfolding. Specific chapters in this release include Protein Aggregation: An Overview, Pathways of Amyloid Fibril Formation and Aggregation, Factors Influencing Amyloid Fibril Formation, Morphological Features and Types of Aggregated Structures, Each big journey starts with a first step: Importance of Oligomerization, Liquid-Liquid Phase Separation as Triggering Factor of Fibril Formation, and more. Additional sections cover Experimental Techniques for Detecting and Evaluating the Amyloid Fibrils, Prediction of Protein Aggregation, Amyloid Fibril Cytotoxicity and Associated Disorders, Inhibitors of Amyloid Fibril Formation, Therapeutic Approaches in Proteinopathies, Functional Amyloids, Biotechnological Applications of Amyloid Fibrils, and The Hidden World of Protein Aggregation. Provides an introduction to the folding of protein and associated conditions leading to aggregation and linked pathology Discusses structural biology and computational methodologies for analysis of protein (mis)folding and aggregation Describes functional amyloids and their biotechnological applications
Book Synopsis Protein Amyloid Aggregation by : David Eliezer
Download or read book Protein Amyloid Aggregation written by David Eliezer and published by Humana. This book was released on 2015-10-11 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.
Book Synopsis Amyloid, Prions, and Other Protein Aggregates by :
Download or read book Amyloid, Prions, and Other Protein Aggregates written by and published by Elsevier. This book was released on 1999-09-22 with total page 861 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates.The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
Book Synopsis Time-resolved Fluorescence Studies of Protein Aggregation Leading to Amyloid Formation by : Jason Thomas Giurleo
Download or read book Time-resolved Fluorescence Studies of Protein Aggregation Leading to Amyloid Formation written by Jason Thomas Giurleo and published by . This book was released on 2008 with total page 345 pages. Available in PDF, EPUB and Kindle. Book excerpt: Aggregation of soluble polypeptides or proteins into insoluble amyloid fibrils containing the cross-beta structural motif has been observed in the progression of over 20 diseases. Self-assembly mechanisms have been proposed but are not well-established. Recent evidence has shifted some of the focus from amyloid fibrils to prefibrillar amyloidogenic aggregates as the cause of disease symptoms. We used time-resolved non-covalent fluorescence labeling to follow the conformational changes occurring in a model protein (beta-lactoglobulin) during amyloid aggregation. The data was analyzed using a novel model-free globally regularized fitting technique. This reduction of model space allowed for stable fitting and the ability to identify intermediate species. An aggregation model was then proposed. In the second half of this thesis, our attention is shifted to alpha-synuclein (alphaSyn). alphaSyn is the majority protein component of the fibrillar inclusion bodies found in brains of Parkinson's disease patients. We have begun a set of fluorescence lifetime experiments using covalent and non-covalent labeling schemes to elucidate the dynamic, conformational and aggregation properties of alphaSyn.
Book Synopsis Exploring New Findings on Amyloidosis by : Ana Maria Fernandez-Escamilla
Download or read book Exploring New Findings on Amyloidosis written by Ana Maria Fernandez-Escamilla and published by BoD – Books on Demand. This book was released on 2016-08-24 with total page 348 pages. Available in PDF, EPUB and Kindle. Book excerpt: Amyloid protein aggregates are involved in ''protein-misfolding diseases'' of enormous social and economic impact, still with no effective therapies. The most prevalent amyloid pathologies are related to neurodegenerative diseases, but amyloidosis also affects other organs. The majority of the studies includes serious health connotations on amyloids. However, not all amyloid fibers play a detrimental role in host. An increasing number of studies shows an important beneficial role as ''functional amyloids''. This book opens an exciting door to provide up-to-date information about the function and the mechanisms of the amyloid formation process from the structural, biophysical, biomedical, and nanotechnological perspective, combining the new findings on toxic and functional amyloids studies using theoretical and experimental approaches to fight against amyloid-based diseases.
Book Synopsis Molecular Pathology of Alzheimer's Disease by : Rudy Castellani
Download or read book Molecular Pathology of Alzheimer's Disease written by Rudy Castellani and published by Biota Publishing. This book was released on 2013-10-01 with total page 93 pages. Available in PDF, EPUB and Kindle. Book excerpt: Alzheimer’s Disease is characterized pathologically by two principal hallmark lesions: the senile plaque and the neurofibrillary tangle. Since the identification of each over 100 years ago, the major protein components have been elucidated. This has led in turn to the elaboration of metabolic cascades involving amyloid-β production in the case of the senile plaque, and phosphorylated-tau protein in the case of the neurofibrillary tangle. The pathogenesis and histogenesis of each have been the source of extensive investigation and some controversy in recent years, as both cascades have been implicated in the pathogenesis of Alzheimer’s Disease, relied upon in the diagnostic criteria for Alzheimer’s Disease at autopsy, and targeted for therapeutic intervention. With the accumulation of data and expansion of knowledge of the molecular biology of Alzheimer’s Disease, it appears that the enthusiasm for successful intervention has been premature. In this book, we detail the discovery and characterization of the major pathological lesions, their associated molecular biology, their relationship to clinical disease, and potential fundamental errors in understanding that may be leading scientific investigators in unintended directions.
Book Synopsis Fibrous Proteins: Amyloids, Prions and Beta Proteins by : John M. Squire
Download or read book Fibrous Proteins: Amyloids, Prions and Beta Proteins written by John M. Squire and published by Elsevier. This book was released on 2006-12-12 with total page 329 pages. Available in PDF, EPUB and Kindle. Book excerpt: Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial. Fibrous proteins act as molecular scaffolds in cells providing the supporting structures of our skeletons, bones, tendons, cartilage, and skin. They define the mechanical properties of our internal hollow organs such as the intestines, heart, and blood vessels. This volume covers such topics as Beta-Structures in Fibrous Proteins; B-Silks: Enhancing and Controlling Aggregation; Beta-Rolls, Beta-Helices and Other Beta-Solenoid Proteins; Natural Triple B-Stranded Fibrous Folds; Structure, Function and Amyloidogenesis of Fungal Prions: Filament Polymorphism and Prion Variants; X-Ray Fiber and powder Diffraction of PRP Prion Peptides; From the Polymorphism of Amyloid Fibrils to Their Assembly Mechanism and Cytotoxicity; Structural Models of Amyloid-like Fibrils.
Download or read book Tau oligomers written by Jesus Avila and published by Frontiers E-books. This book was released on 2014-08-18 with total page 114 pages. Available in PDF, EPUB and Kindle. Book excerpt: Neurofibrillary tangles (NFTs) composed of intracellular aggregates of tau protein are a key neuropathological feature of Alzheimer’s Disease (AD) and other neurodegenerative diseases, collectively termed tauopathies. The abundance of NFTs has been reported to correlate positively with the severity of cognitive impairment in AD. However, accumulating evidences derived from studies of experimental models have identified that NFTs themselves may not be neurotoxic. Now, many of tau researchers are seeking a “toxic” form of tau protein. Moreover, it was suggested that a “toxic” tau was capable to seed aggregation of native tau protein and to propagate in a prion-like manner. However, the exact neurotoxic tau species remain unclear. Because mature tangles seem to be non-toxic component, “tau oligomers” as the candidate of “toxic” tau have been investigated for more than one decade. In this topic, we will discuss our consensus of “tau oligomers” because the term of “tau oligomers” [e.g. dimer (disulfide bond-dependent or independent), multimer (more than dimer), granular (definition by EM or AFM) and maybe small filamentous aggregates] has been used by each researchers definition. From a biochemical point of view, tau protein has several unique characteristics such as natively unfolded conformation, thermo-stability, acid-stability, and capability of post-translational modifications. Although tau protein research has been continued for a long time, we are still missing the mechanisms of NFT formation. It is unclear how the conversion is occurred from natively unfolded protein to abnormally mis-folded protein. It remains unknown how tau protein can be formed filaments [e.g. paired helical filament (PHF), straight filament and twisted filament] in cells albeit in vitro studies confirmed tau self-assembly by several inducing factors. Researchers are still debating whether tau oligomerization is primary event rather than tau phosphorylation in the tau pathogenesis. Inhibition of either tau phosphorylation or aggregation has been investigated for the prevention of tauopathies, however, it will make an irrelevant result if we don’t know an exact target of neurotoxicity. It is a time to have a consensus of definition, terminology and methodology for the identification of “tau oligomers”.
Book Synopsis Lipids and Cellular Membranes in Amyloid Diseases by : Raz Jelinek
Download or read book Lipids and Cellular Membranes in Amyloid Diseases written by Raz Jelinek and published by John Wiley & Sons. This book was released on 2011-04-27 with total page 431 pages. Available in PDF, EPUB and Kindle. Book excerpt: Addressing one of the biggest riddles in current molecular cell biology, this ground-breaking monograph builds the case for the crucial involvement of lipids and membranes in the formation of amyloid deposits. Tying together recent knowledge from in vitro and in vivo studes, and built on a sound biophysical and biochemical foundation, this overview brings the reader up to date with current models of the interplay between membranes and amyloid formation. Required reading for any researcher interested in amyloid formation and amyloid toxicity, and possible avenues for the prevention or treatment of neurodegenerative disorders. From the contents: * Interactions of Alpha-Synuclein with Lipids * Interaction of hIAPP and its Precursors with Membranes * Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine * The Role of Lipid Rafts in Alzheimer's Disease * Alzheimer's Disease as a Membrane-Associated Enzymopathy of Beta-Amyloid Precursor Protein (APP) Secretases * Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by Beta-Amyloid in Alzheimer's Disease * Membrane Changes in BSE and Scrapie * Experimental Approaches and Technical Challenges for Studying Amyloid-Membrane Interactions and more
Book Synopsis Genetic Causes of Amyloid Fibrils and Their Structures by : Gregory M Rosenberg
Download or read book Genetic Causes of Amyloid Fibrils and Their Structures written by Gregory M Rosenberg and published by . This book was released on 2023 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: The conversion of human proteins into the highly ordered fibrillar aggregates known as amyloid fibrils is implicated in a wide range of diseases. The number of proteins known to exhibit this activity is constantly growing and the molecular mechanisms that lead to amyloid aggregation are not fully understood. I focus on genetic mutations as a mechanism by which to predict novel amyloidogenic proteins. I also examine how mutations can explain some structural features of amyloid fibrils formed by mutant proteins. I developed a computational method for predicting previously unknown amyloidogenic proteins by calculating the propensity of disease mutations to induce amyloid aggregation. This method, called Identification of Mutations Promoting Amyloidogenic Transitions (IMPAcT), identified protein TFG as a novel amyloidogenic protein. I biochemically validated the amyloidogenic nature of mutant protein TFG and determined the structures of the mutant amyloid fibrils, demonstrating the direct and indirect influence of each mutation on the structure and stability of the fibrils. Lastly, I composed a literature review of the mechanisms by which mutations drive the conversion to an amyloid fibril and influence the resulting molecular structures. This body of research expands our understanding of amyloid proteins and opens avenues for further study of the relationship between genetics and amyloids.This dissertation includes three supplementary files. Chapter 2 has two supplementary spreadsheets: Table S2-1 is a spreadsheet containing information regarding all the candidate mutations identified by the IMPAcT method; Table S2-2 is a spreadsheet containing the results of a statistical test on patterns in the kinds of mutations which were predicted to be amyloidogenic by the IMPAcT method. Chapter 4 has one supplementary spreadsheet: Table S4-1 is a spreadsheet containing relevant information on all pathogenic amyloid proteins considered in the review.
